Screening of isolated DNA for sequences released from anchorage sites in nuclear matrix

Poly(ADP-Ribose) Biosynthesis

“…These investigators convincingly demonstrated that poly(ADP-ribose)polymerase is closely associated with the nuclear matrix ("scaffold") of interphase cells. Neuer and Werner 1985). These results are particularly interesting in view of a newly evolving concept suggesting that actively transcribing genes and replicating DNA domains temporarily associate with components of the nuclear matrix (e.g.…”

DNA end-independent activation of DNA-PK mediated via association with the DNA-binding protein C1D

“…Highly stable nonhistone proteins that are bound to DNA tightly have been identified in various systems, including insects, plants, and mammalian cells (Krauth and Werner 1979;Capesius et al 1980;Bodnar et al 1983;Avramova and Tsanev 1987). Although the biological functions for these proteins are still largely obscure, it is noteworthy that some have been reported to be associated with highly repetitive DNA sequences and to be involved in targeting a subset of genomic DNA to the nuclear matrix (Neuer and Werner 1985;NeuerNitsche et al 1988;Werner and Neuer-Nitsche 1989;Pfutz et al 1992). This is of particular interest in regard to the results described herein, as the nuclear matrix is thought to provide the structural framework for nuclear/ chromatin organization, and has been shown to associate with several nuclear metabolic processes including DNA replication, transcription, RNA splicing, topoisomerase activity, nucleotide excision repair, and DNA DSB repair (Berezney 1984;Cockerill and Garrard 1986;Nelson et al 1986;Verheijen et al 1988;Jackson 1991;Kaufman and Shaper 1991;Yasui et al 1991Yasui et al , 1994Korte and Yasui 1993;Johnston and Bryant 1994;Koehler and Hanawalt 1996).…”

Chemical and enzymatic analysis of covalent bonds between peptides and chromosomal DNA

“…However, it is highly likely that the linkage-groups characterized in this paper reflect the binding sites of polypeptides that have been detected in highly purified DNA preparations from different organisms and by different techniques including (1) digestion of milligram-amounts of highly purified DNA by nucleases followed by examination of the polypeptides by SDS / polyacrylamide gel electrophoresis and Coomassie blue staining [4], (2) radioiodination of DNA preparations followed by degradation of DNA and analysis of the residual radiolabelled polypeptides by combined SDS / polyacrylamide gel electrophoresis and autoradiography [24], and (3) radiolabelling of polypeptides associated with DNA by nicktranslation in presence of c[32P]dCTP and analysis of the polypeptides and their associated residual radiolabelled nucleotides by combined SDS / polyacrylamide gel electrophoresis and autoradiography [25]. DNA-polypeptide complexes of this kind were found in DNA at an average distance of -10 kbp [26], however, there is evidence indicating that the distribution along DNA is non-random [27,28]. Since the physico-chemical characteristics of the polypeptides involved in the complexes are different from those of topoisomerases it has been concluded that at least the majority of the covalent complexes do not reflect topoisomerase molecules transiently bound to DNA [29].…”